Carboxypeptidase Taq | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.4.17.19 | ||||||||
CAS no. | 9031-98-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme. This enzyme catalyses the following chemical reaction
- Release of a C-terminal amino acid with broad specificity, except for -Pro
This 56-kDa enzyme is isolated from Thermus aquaticus.
References
- Lee SH, Minagawa E, Taguchi H, Matsuzawa H, Ohta T, Kaminogawa S, Yamauchi K (November 1992). "Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". Bioscience, Biotechnology, and Biochemistry. 56 (11): 1839–44. doi:10.1271/bbb.56.1839. PMID 1369078.
- Lee SH, Taguchi H, Yoshimura E, Minagawa E, Kaminogawa S, Ohta T, Matsuzawa H (August 1994). "Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli". Bioscience, Biotechnology, and Biochemistry. 58 (8): 1490–5. doi:10.1271/bbb.58.1490. PMID 7765282.
External links
- Carboxypeptidase+Taq at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: proteases (EC 3.4) | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
3.4.11-19: Exopeptidase |
| ||||||||||||||
3.4.21-25: Endopeptidase | |||||||||||||||
3.4.99: Unknown |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|